Acyl aminoacyl peptidases are two-domain proteins composed by a C-terminal catalytic α/β-hydrolase domain and by an N-terminal β-propeller domain connected through a structural element that is at the N-terminus in sequence but participates in the 3D structure of the C-domain. We investigated about the structural and functional interplay between the two domains and the bridge structure (in this case a single helix named α1-helix) in the cold-adapted enzyme from Sporosarcina psychrophila (SpAAP) using both protein variants in which entire domains were deleted and proteins carrying substitutions in the α1-helix. We found that in this enzyme the inter-domain connection dramatically affects the stability of both the whole enzyme and the β-propeller. The α1-helix is required for the stability of the intact protein, as in other enzymes of the same family; however in this psychrophilic enzyme only, it destabilizes the isolated β-propeller. A single charged residue (E10) in the α1-helix plays a major role for the stability of the whole structure. Overall, a strict interaction of the SpAAP domains seems to be mandatory for the preservation of their reciprocal structural integrity and may witness their co-evolution

Parravicini, F., Natalello, A., Papaleo, E., DE GIOIA, L., Doglia, S., Lotti, M., et al. (2013). Reciprocal influence of protein domains in the cold-adapted acyl aminoacyl peptidase from Sporosarcina psychrophila. PLOS ONE, 8(2), 1-11 [10.1371/journal.pone.0056254].

Reciprocal influence of protein domains in the cold-adapted acyl aminoacyl peptidase from Sporosarcina psychrophila

PARRAVICINI, FEDERICA;NATALELLO, ANTONINO;PAPALEO, ELENA;DE GIOIA, LUCA;DOGLIA, SILVIA MARIA;LOTTI, MARINA;BROCCA, STEFANIA
2013

Abstract

Acyl aminoacyl peptidases are two-domain proteins composed by a C-terminal catalytic α/β-hydrolase domain and by an N-terminal β-propeller domain connected through a structural element that is at the N-terminus in sequence but participates in the 3D structure of the C-domain. We investigated about the structural and functional interplay between the two domains and the bridge structure (in this case a single helix named α1-helix) in the cold-adapted enzyme from Sporosarcina psychrophila (SpAAP) using both protein variants in which entire domains were deleted and proteins carrying substitutions in the α1-helix. We found that in this enzyme the inter-domain connection dramatically affects the stability of both the whole enzyme and the β-propeller. The α1-helix is required for the stability of the intact protein, as in other enzymes of the same family; however in this psychrophilic enzyme only, it destabilizes the isolated β-propeller. A single charged residue (E10) in the α1-helix plays a major role for the stability of the whole structure. Overall, a strict interaction of the SpAAP domains seems to be mandatory for the preservation of their reciprocal structural integrity and may witness their co-evolution
Articolo in rivista - Articolo scientifico
Cold-adapted enzymes, protein domains, beta-propeller, alpha/beta hydrolase fold
English
2013
8
2
1
11
e56254
none
Parravicini, F., Natalello, A., Papaleo, E., DE GIOIA, L., Doglia, S., Lotti, M., et al. (2013). Reciprocal influence of protein domains in the cold-adapted acyl aminoacyl peptidase from Sporosarcina psychrophila. PLOS ONE, 8(2), 1-11 [10.1371/journal.pone.0056254].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/44462
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